CAS3_THET8
ID CAS3_THET8 Reviewed; 920 AA.
AC Q53VY2;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=CRISPR-associated endonuclease/helicase Cas3;
DE EC=3.1.-.-;
DE EC=3.6.4.-;
DE AltName: Full=CRISPR-associated ssDNA endonuclease/helicase Cas3;
GN Name=cas3; OrderedLocusNames=TTHB187;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 6-260 IN PRESENCE AND ABSENCE OF
RP NI(2+), FUNCTION AS A SSDNA ENDONUCLEASE, ACTIVITY REGULATION, COFACTOR,
RP AND MUTAGENESIS OF HIS-24; HIS-69; ASP-70; LYS-73; HIS-105; HIS-137;
RP HIS-138 AND ASP-205.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21775431; DOI=10.1074/jbc.m111.270017;
RA Mulepati S., Bailey S.;
RT "Structural and biochemical analysis of nuclease domain of clustered
RT regularly interspaced short palindromic repeat (CRISPR)-associated protein
RT 3 (Cas3).";
RL J. Biol. Chem. 286:31896-31903(2011).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3
CC plus Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity. The N-terminal domain (residues 6-260) acts as a ssDNA
CC endonuclease, has no activity on dsDNA. {ECO:0000269|PubMed:21775431}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21775431};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21775431};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:21775431};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:21775431};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21775431};
CC Note=The ssDNA endonuclease activity (residues 6-260) is stimulated by
CC Mn(2+), Co(2+), Ni(2+), Cu(2+) and Zn(2+), but not by Mg(2+) or Ca(2+).
CC A Ni(2+) ion is seen in crystals upon soaking.
CC {ECO:0000269|PubMed:21775431};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, Mg(2+) and Ca(2+).
CC {ECO:0000269|PubMed:21775431}.
CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain and
CC a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the
CC domains are swapped, in others they are encoded separately.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC nuclease Cas3-HD family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC helicase Cas3 family. {ECO:0000305}.
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DR EMBL; AP008227; BAD71983.1; -; Genomic_DNA.
DR RefSeq; WP_011229117.1; NC_006462.1.
DR RefSeq; YP_145426.1; NC_006462.1.
DR PDB; 3SK9; X-ray; 1.80 A; A=6-260.
DR PDB; 3SKD; X-ray; 2.00 A; A=6-260.
DR PDBsum; 3SK9; -.
DR PDBsum; 3SKD; -.
DR AlphaFoldDB; Q53VY2; -.
DR SMR; Q53VY2; -.
DR EnsemblBacteria; BAD71983; BAD71983; BAD71983.
DR GeneID; 3167883; -.
DR KEGG; ttj:TTHB187; -.
DR PATRIC; fig|300852.9.peg.2138; -.
DR HOGENOM; CLU_013924_1_0_0; -.
DR OMA; CVCWIRN; -.
DR PhylomeDB; Q53VY2; -.
DR EvolutionaryTrace; Q53VY2; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3210.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035011; Cas3.
DR InterPro; IPR041372; Cas3_C.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47959:SF5; PTHR47959:SF5; 2.
DR Pfam; PF18395; Cas3_C; 1.
DR Pfam; PF18019; HD_6; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01587; cas3_core; 1.
DR TIGRFAMs; TIGR01596; cas3_HD; 1.
DR PROSITE; PS51643; HD_CAS3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Endonuclease; Helicase;
KW Hydrolase; Metal-binding; Nuclease; Nucleotide-binding; Plasmid;
KW Reference proteome.
FT CHAIN 1..920
FT /note="CRISPR-associated endonuclease/helicase Cas3"
FT /id="PRO_0000417609"
FT DOMAIN 14..207
FT /note="HD Cas3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT DOMAIN 274..480
FT /note="Helicase ATP-binding"
FT MOTIF 428..431
FT /note="DEAH box"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 69
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 24
FT /note="H->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 69
FT /note="H->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 70
FT /note="D->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 73
FT /note="K->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 105
FT /note="H->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 137
FT /note="H->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 138
FT /note="H->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT MUTAGEN 205
FT /note="D->A: Loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:21775431"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:3SK9"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:3SK9"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3SK9"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:3SK9"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3SK9"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:3SK9"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3SK9"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:3SK9"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3SK9"
SQ SEQUENCE 920 AA; 102127 MW; D0A13064DD5B8191 CRC64;
MSVEEAALAL WAKSGNPFHP LLAHMLDTAA VALAVLRMEP PRTRALYAED WGLPEEGALA
WAAALVGLHD LGKASPVFQA GWEEGKERVQ RAGLPFGELL DWVAHGVFTE LFLRRLLKEK
GLPERAANDL AAALGAHHGF PANAEEKSRA RRHLRTEDPL WKEARRWLLE EVFRRLGAPL
PPSQGNGEAR PEAVLRVMAL ASFADWVASD PSLFPYGRDP RRGDYLKEAL RLAQEALNRL
GWPAFAKAQR REFGELFPYI PKPNALQESV PALLEGACTP VLLLVEAPMG MGKTEAALYA
HHLLQAGLGH RGLYVALPTQ ATANGLFPRV RGFLERLGEG SRLELQLQHG TALLNPHYAG
LLERAAPRQV GEEEEGGAVA SAWFSARKRA MLAPYGVGTL DQALLGVLRV KHHFVRLWGL
MNRVVVLDEV HAYDVYTSGL LQALLRWLRA LGSSAVVMTA TLPPSRRRAL LEAWAGEEVE
GQDLGPYPRV VLVGEGVKAR SLPPAREVEV ALEVLREVDV EPLAQRLKGA LPGAVGAIVN
TVDRAQDLYR ALGEGTPLTL EELARRLGGI SGGQAWEEVR QALPERGGEV VGKVLTDGTL
VFLLHARFPA EERALRGSVV LALFGKGGPR PPRAILVATQ VAEQSLDLDF DLLYTDLAPI
DLLFQRSGRL HRHERPRPEE HARPRLLLGV PEDLDFGKPL YWDKVYEDYV LLATWRALSG
RDRLRVPGDL EALLEEIYEG ENPESFPEGL RERAKKSLKA LQERRDREAN TARRLSLSEL
DRLLAYWDEG ALVAQERLED DEEKAETQRL LTRLGDPSVA VVPLFRVGEG LFLDREGRRR
APLKGEVSRE EAEALFRRAV RLSRFPLPQE LLKEEPPPAW RKSGLLRGLR PLEVGRVFRS
GERAFQVELD PELGVVYLPV
